5VJ0
Crystal Structure of heme-containing DyP Type Peroxidase from Enterobacter lignolyticus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue HEM A 500 |
| Chain | Residue |
| A | ASP137 |
| A | ARG197 |
| A | HIS215 |
| A | VAL219 |
| A | ARG232 |
| A | LEU246 |
| A | PHE248 |
| A | GLN261 |
| A | LEU262 |
| A | MET265 |
| A | MET276 |
| A | VAL142 |
| A | HOH653 |
| A | HOH658 |
| A | ASP143 |
| A | GLY144 |
| A | THR145 |
| A | GLU146 |
| A | GLN174 |
| A | TRP176 |
| A | HIS178 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue HEM B 500 |
| Chain | Residue |
| B | ASP137 |
| B | VAL142 |
| B | ASP143 |
| B | GLY144 |
| B | THR145 |
| B | GLU146 |
| B | GLN174 |
| B | TRP176 |
| B | HIS178 |
| B | ARG197 |
| B | HIS215 |
| B | ASP220 |
| B | ARG232 |
| B | LEU246 |
| B | PHE248 |
| B | GLN261 |
| B | MET265 |
| B | MET276 |
| B | THR280 |
| B | HOH636 |
| B | HOH663 |
| B | HOH732 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue HEM C 500 |
| Chain | Residue |
| C | ASP137 |
| C | VAL142 |
| C | ASP143 |
| C | GLY144 |
| C | THR145 |
| C | GLU146 |
| C | GLN174 |
| C | TRP176 |
| C | HIS178 |
| C | ARG197 |
| C | HIS215 |
| C | VAL219 |
| C | ARG232 |
| C | LEU246 |
| C | PHE248 |
| C | GLN261 |
| C | MET276 |
| C | THR280 |
| C | HOH616 |
| C | HOH672 |
| C | HOH764 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue HEM D 500 |
| Chain | Residue |
| D | ASP137 |
| D | VAL142 |
| D | ASP143 |
| D | GLY144 |
| D | THR145 |
| D | GLU146 |
| D | GLN174 |
| D | TRP176 |
| D | HIS178 |
| D | ARG197 |
| D | HIS215 |
| D | VAL219 |
| D | ARG232 |
| D | LEU246 |
| D | PHE248 |
| D | GLN261 |
| D | MET265 |
| D | MET276 |
| D | HOH661 |
| D | HOH665 |
| D | HOH788 |
